Abstract:
:Ionotropic glutamate receptors (iGluRs) are responsible for most of the fast excitatory communication between neurons in our brain. The GluD2 receptor is a puzzling member of the iGluR family: It is involved in synaptic plasticity, plays a role in human diseases, e.g. ataxia, binds glycine and D-serine with low affinity, yet no ligand has been discovered so far that can activate its ion channel. In this study, we show that the hinge region connecting the two subdomains of the GluD2 ligand-binding domain is responsible for the low affinity of D-serine, by analysing GluD2 mutants with electrophysiology, isothermal titration calorimetry and molecular dynamics calculations. The hinge region is highly variable among iGluRs and fine-tunes gating activity, suggesting that in GluD2 this region has evolved to only respond to micromolar concentrations of D-serine.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Tapken D,Steffensen TB,Leth R,Kristensen LB,Gerbola A,Gajhede M,Jørgensen FS,Olsen L,Kastrup JSdoi
10.1038/srep46145subject
Has Abstractpub_date
2017-04-07 00:00:00pages
46145issn
2045-2322pii
srep46145journal_volume
7pub_type
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